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Papers In Press, published online ahead of print August 11, 2006
J. Biol. Chem, 10.1074/jbc.M606992200
Submitted on July 24, 2006
Accepted on August 11, 2006

Phosphorylation and upregulation of diacylglycerol kinase gamma via its interaction with protein kinase Cgamma

Yasuto Yamaguchi, Yasuhito Shirai, Takehiro Matsubara, Koh-ichi Sanse, Masamitsu Kuriyama, Noriko Ohshiro, Ken-ichi Yoshino, Kazuyoshi Yonezawa, Yoshitaka Ono, and Naoaki Saito

Laboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University, Kobe 657-8501

Corresponding Author: naosaito{at}kobe-u.ac.jp

Diacylglycerol (DAG) acts as an allosteric activator of protein kinase C (PKC), and is converted to phosphatidic acid by DAG kinase (DGK). DGK, therefore, is thought to be a negative regulator of PKC activation. Here, we show molecular mechanisms of functional coupling of the two kinases. gamma PKC directly associated with DGKgamma through its accessory domain (AD), depending on Ca2+ as well as phosphatidylserine/ diolein in vitro. Mass spectrometric analysis and mutation studies revealed that gamma PKC phosphorylated Ser776 and Ser779 in the AD of DGKgamma . The phosphorylation by gamma PKC resulted in activation of DGKgamma because a DGKgamma mutant in which Ser776 and Ser779 were substituted with glutamic acid to mimic phosphorylation exhibited significantly higher activity compared to wild type DGKgamma and an unphosphorylatable DGKgamma mutant. Importantly, the interaction of the two kinases and the phosphorylation of DGKgamma by gamma PKC could be confirmed in vivo, and over-expression of the AD of DGKgamma inhibited re-translocation of gamma PKC. These results demonstrate that localization and activation of the functionally-correlated kinases, gamma PKC and DGKgamma are spatio-temporally orchestrated by their direct association and phosphorylation, contributing to subtype-specific regulation of DGKgamma and DAG signaling.


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